title: Hairpin folding behavior of mixed α/β-peptides in aqueous solution.
abstract: The invention of new strategies for the design of protein-mimetic oligomers that manifest the folding encoded in natural amino acid sequences is a significant challenge. In contrast to the α-helix, mimicry of protein β-sheets is less understood. We report here the aqueous folding behavior of a prototype α-peptide hairpin model sequence varied at cross-strand positions by incorporation of 16 different β-amino acid monomers. Our results provide a folding propensity scale for β-residues in a protein β-sheet context as well as high-resolution structures of several mixed-backbone α/β-peptide hairpins in water.
authors.affiliation: Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA.
authors.forename: George A
authors.initials: GA
authors.lastname: Lengyel
authors.forename: Rebecca C
authors.initials: RC
authors.lastname: Frank
authors.forename: W Seth
authors.initials: WS
authors.lastname: Horne
mesh_terms: D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012996:Solutions; D014867:Water / Q000737:chemistry
chemical_list: D010455:Peptides; D012996:Solutions; D014867:Water